Cooperativity and Folding Kinetics in a Multidomain Protein with Interwoven Chain Topology
Author:
Affiliation:
1. Department of Physics, Beijing Normal University, Beijing 100875, China
2. Department of Chemistry, The University of Texas at Austin, Austin, Texas 78712, United States
Funder
Division of Chemistry
China Scholarship Council
National Natural Science Foundation of China
the Collie-Welch Regents chair
Publisher
American Chemical Society (ACS)
Subject
General Chemical Engineering,General Chemistry
Link
https://pubs.acs.org/doi/pdf/10.1021/acscentsci.2c00140
Reference48 articles.
1. The folding and evolution of multidomain proteins
2. Reversible Unfolding of Individual Titin Immunoglobulin Domains by AFM
3. Nucleation, Rapid Folding, and Globular Intrachain Regions in Proteins
4. The folding cooperativity of a protein is controlled by its chain topology
5. Single-molecule fluorescence spectroscopy maps the folding landscape of a large protein
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